Information on EC 3.1.2.14 - oleoyl-[acyl-carrier-protein] hydrolase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

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EC NUMBER
COMMENTARY hide
3.1.2.14
-
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RECOMMENDED NAME
GeneOntology No.
oleoyl-[acyl-carrier-protein] hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an oleoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + oleate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acyl-[acyl-carrier protein] thioesterase pathway
-
-
bacterial bioluminescence
-
-
cis-vaccenate biosynthesis
-
-
mycobacterial sulfolipid biosynthesis
-
-
oleate biosynthesis I (plants)
-
-
palmitate biosynthesis I (animals and fungi)
-
-
palmitate biosynthesis II (bacteria and plants)
-
-
palmitoleate biosynthesis I (from (5Z)-dodec-5-enoate)
-
-
palmitoleate biosynthesis II (plants and bacteria)
-
-
petroselinate biosynthesis
-
-
stearate biosynthesis II (bacteria and plants)
-
-
arachidonate biosynthesis
-
-
cis-vaccenate biosynthesis
-
-
palmitate biosynthesis
-
-
Fatty acid biosynthesis
-
-
Metabolic pathways
-
-
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SYSTEMATIC NAME
IUBMB Comments
oleoyl-[acyl-carrier protein] hydrolase
Acts on acyl-carrier-protein thioesters of fatty acids from C12 to C18, but the derivative of oleic acid is hydrolysed much more rapidly than any other compound tested.
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CAS REGISTRY NUMBER
COMMENTARY hide
105669-84-9
-
68009-83-6
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv. Pusa Bold
SwissProt
Manually annotated by BRENDA team
Br FatA1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Cs FatA1
-
-
Manually annotated by BRENDA team
isozymes AH1, AH2, AH3
-
-
Manually annotated by BRENDA team
var. mesostemon
SwissProt
Manually annotated by BRENDA team
Ch FatA1 and Ch FatB1 and Ch FatB2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Elaeis sp.
oil palm
-
-
Manually annotated by BRENDA team
Gm FatA1 and Gm FatA2
-
-
Manually annotated by BRENDA team
cv. Paymaster HS26, gene FatB
SwissProt
Manually annotated by BRENDA team
gene fatA1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment of precursor
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
var. Fuerte, avocado
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Carr
SwissProt
Manually annotated by BRENDA team
Carr
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Um FatB1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
the main change in the Escherichia coli fatty acid composition when CsFatA is expressed is the reduction in unsaturated fatty acids, mainly cis-vaccenic acid (18:1 omega7). This reduction is compensated for by an increase of palmitoleic acid (16:1 omega7); the main change in the Escherichia coli fatty acid composition when CsFatB is expressed is a decrease in saturated fatty acids and in particular, that of palmitic acid (16:0) that is compensated for with an increase in stearic acid (18.0)
physiological function
-
deduced amino acid sequence displays high homology to choroplastic palmitoyl-acyl carrier protein thioesterases from other plants
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acyl-[acyl-carrier protein] + H2O
?
show the reaction diagram
decanoyl-[acyl-carrier protein] + H2O
decanoic acid + acyl-carrier protein
show the reaction diagram
dodecenoyl-[acyl-carrier protein] + H2O
dodecenoic acid + acyl-carrier protein
show the reaction diagram
-
-
-
?
lauroyl-CoA + H2O
lauric acid + CoA
show the reaction diagram
-
-
-
?
lauroyl-[acyl-carrier protein] + H2O
lauric acid + acyl-carrier protein
show the reaction diagram
myristoleoyl-[acyl-carrier protein] + H2O
myristoleic acid + acyl-carrier protein
show the reaction diagram
myristoyl-[acyl-carrier protein] + H2O
myristic acid + acyl-carrier protein
show the reaction diagram
oleoyl-[acyl-carrier protein] + H2O
?
show the reaction diagram
-
endpoint of de novo fatty acid synthesis in plastids
-
-
-
oleoyl-[acyl-carrier protein] + H2O
acyl-carrier protein + oleic acid
show the reaction diagram
oleoyl-[acyl-carrier protein] + H2O
oleate + acyl-carrier protein
show the reaction diagram
-
substrates are long chain acyl-acyl carrier proteins
-
?
oleoyl-[acyl-carrier protein] + H2O
oleic acid + acyl-carrier protein
show the reaction diagram
oleoyl-[acyl-carrier protein] + H2O
[acyl-carrier protein] + oleate
show the reaction diagram
oleoyl-[acyl-carrier-protein] + H2O
oleic acid + acyl-carrier-protein
show the reaction diagram
palmitoleoyl-[acyl-carrier protein] + H2O
acyl-carrier protein + palmitoleic acid
show the reaction diagram
-
-
-
?
palmitoleoyl-[acyl-carrier protein] + H2O
palmitoleate + acyl-carrier protein
show the reaction diagram
palmitoleoyl-[acyl-carrier protein] + H2O
palmitoleic acid + acyl-carrier protein
show the reaction diagram
palmitoleoyl-[acyl-carrier protein] + H2O
[acyl-carrier protein] + palmitoleate
show the reaction diagram
palmitoyl-[acyl-carrier protein] + H2O
acyl-carrier protein + palmitic acid
show the reaction diagram
palmitoyl-[acyl-carrier protein] + H2O
palmitate + acyl-carrier protein
show the reaction diagram
palmitoyl-[acyl-carrier protein] + H2O
palmitic acid + acyl-carrier protein
show the reaction diagram
palmitoyl-[acyl-carrier protein] + H2O
[acyl-carrier protein] + palmitate
show the reaction diagram
-
-
-
-
?
palmitoyl-[acyl-carrier-protein] + H2O
palmitic acid + acyl-carrier-protein
show the reaction diagram
12% of the activity with stearoyl-[acyl-carrier-protein]
-
-
?
stearoyl-ACP + H2O
stearate + acyl-carrier protein
show the reaction diagram
-
-
-
-
?
stearoyl-[acyl-carrier protein] + H2O
?
show the reaction diagram
-
synthesis of fatty acids for wax biosynthesis
-
-
-
stearoyl-[acyl-carrier protein] + H2O
acyl-carrier protein + stearic acid
show the reaction diagram
stearoyl-[acyl-carrier protein] + H2O
stearate + acyl-carrier protein
show the reaction diagram
-
-
-
?
stearoyl-[acyl-carrier protein] + H2O
stearic acid + acyl-carrier protein
show the reaction diagram
stearoyl-[acyl-carrier protein] + H2O
[acyl-carrier protein] + stearate
show the reaction diagram
stearoyl-[acyl-carrier-protein] + H2O
stearic acid + acyl-carrier-protein
show the reaction diagram
-
-
-
?
undecanoyl-[acyl-carrier protein] + H2O
undecanoic acid + acyl-carrier protein
show the reaction diagram
-
-
-
?
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acyl-[acyl-carrier protein] + H2O
?
show the reaction diagram
oleoyl-[acyl-carrier protein] + H2O
?
show the reaction diagram
-
endpoint of de novo fatty acid synthesis in plastids
-
-
-
oleoyl-[acyl-carrier protein] + H2O
oleic acid + acyl-carrier protein
show the reaction diagram
oleoyl-[acyl-carrier protein] + H2O
[acyl-carrier protein] + oleate
show the reaction diagram
palmitoyl-[acyl-carrier protein] + H2O
palmitate + acyl-carrier protein
show the reaction diagram
palmitoyl-[acyl-carrier protein] + H2O
palmitic acid + acyl-carrier protein
show the reaction diagram
stearoyl-[acyl-carrier protein] + H2O
?
show the reaction diagram
-
synthesis of fatty acids for wax biosynthesis
-
-
-
stearoyl-[acyl-carrier protein] + H2O
stearic acid + acyl-carrier protein
show the reaction diagram
Q9SQI3
-
-
?
additional information
?
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
5,5'-dithiobis(2-nitrobenzoate)
diethyldicarbonate
-
-
iodoacetamide
-
-
N-ethylmaleimide
-
-
oleoyl-[acyl-carrier protein]
-
competitive to other acyl-[acyl-carrier protein] substrates
palmitoyl-[acyl-carrier protein]
-
competitive to other acyl-[acyl-carrier protein] substrates
stearoyl-[acyl-carrier protein]
-
competitive to other acyl-[acyl-carrier protein] substrates
additional information
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006
(9Z)-hexadec-9-enoyl-[acyl-carrier protein]
-
pH 8.0, 22°C, recombinant His-tagged enzyme
0.0023 - 0.004
decanoyl-[acyl-carrier protein]
0.0049
dodecanoyl-[acyl-carrier protein]
-
medium-chain acyl-ACP thioesterase
0.0146 - 0.0166
lauroyl-[acyl-carrier protein]
0.0029 - 0.0139
myristoleoyl-[acyl-carrier protein]
0.0028 - 0.0089
myristoyl-[acyl-carrier protein]
0.0024 - 0.029
octanoyl-[acyl-carrier protein]
0.00008 - 3
oleoyl-[acyl-carrier protein]
0.0006 - 0.0212
oleoyl-[acyl-carrier-protein]
0.0001 - 0.00551
palmitoleoyl-[acyl-carrier protein]
0.00028 - 0.0066
palmitoyl-[acyl-carrier protein]
0.00034 - 0.01
stearoyl-[acyl-carrier protein]
0.0067
undecanoyl-[acyl-carrier protein]
-
-
additional information
additional information
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9
(9Z)-hexadec-9-enoyl-[acyl-carrier protein]
-
pH 8.0, 22°C, recombinant His-tagged enzyme
0.004 - 0.22
myristoleoyl-[acyl-carrier protein]
0.008 - 0.02
myristoyl-[acyl-carrier protein]
0.25 - 11.4
oleoyl-[acyl-carrier protein]
0.032 - 35.6
oleoyl-[acyl-carrier-protein]
0.0016 - 8
palmitoleoyl-[acyl-carrier protein]
0.0005 - 4.4
palmitoyl-[acyl-carrier protein]
0.0002 - 6.08
stearoyl-[acyl-carrier protein]
additional information
additional information
-
recombinant chimeric mutants FatAB and FatBA
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
80 - 19030
oleoyl-[acyl-carrier protein]
50 - 39300
oleoyl-[acyl-carrier-protein]
28 - 48000
palmitoleoyl-[acyl-carrier protein]
3 - 2800
palmitoyl-[acyl-carrier protein]
2 - 1600
stearoyl-[acyl-carrier protein]
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.043
palmitoyl-[acyl-carrier protein], pH 8.0, 22°C
0.144
-
enzyme from leaf epidermis
0.18
-
substrate stearoyl-[acyl-carrier protein], pH 9, 37°C
0.262
palmitoleoyl-[acyl-carrier protein], pH 8.0, 22°C
0.324
stearoyl-[acyl-carrier protein], pH 8.0, 22°C
0.437
oleoyl-[acyl-carrier protein], pH 8.0, 22°C
0.69
-
seed 65 days after flowering, enzyme form PO-FAT
0.744
palmitoleoyl-[acyl-carrier protein], pH 8.0, 22°C
0.778
palmitoyl-[acyl-carrier protein], pH 8.0, 22°C
1.45
stearoyl-[acyl-carrier protein], pH 8.0, 22°C
1.61
oleoyl-[acyl-carrier protein], pH 8.0, 22°C
11
-
isozyme AH1
15
-
recombinant enzyme in Escherichia coli, substrate lauroyl-CoA
192
-
purified enzyme form PO-FAT
1500
-
recombinant enzyme in Escherichia coli, substrate lauroyl-[acyl-carrier-protein]
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
medium-chain acyl-ACP thioesterase
9.3
-
oleoyl-ACP thioesterase
9.8
-
isozymes AH1, AH2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 9
-
medium-chain acyl-ACP thioesterase
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36
-
around 35-37°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.57
-
sequence analysis
6.7
calculated from sequence
8.1
-
amino acid sequence calculation
8.2
-
enzyme form LC-FAT, chromatofocusing
9.7
-
enzyme form PO-FAT, chromatofocusing
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
developing fruit
Manually annotated by BRENDA team
-
stearoyl-ACP thioestersae is predominantly expressed in epidermis
Manually annotated by BRENDA team
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
Elaeis sp.
-
the gene contains a putative transit peptide sequence
-
Manually annotated by BRENDA team
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
F9ULU3
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
medium-chain acyl-ACP thioesterase, gel filtration
33400
-
calculated from cDNA
34800
-
calculated from cDNA
35000
-
2 * 35000, SDS-PAGE
36800
recombinant histidine-tagged FatB, gel filtration
36900
-
x * 41200, about, amino acid sequence calculation, x * 36900, recombinant His-tagged enzyme without signal peptide, SDS-PAGE
37000
-
SDS-PAGE
37250
-
calculation from sequence of cDNA
37520
recombinant histidine-tagged FatA, gel filtration
38000
-
2 * 38000, SDS-PAGE
40500
-
SDS-PAGE
41200
-
x * 41200, about, amino acid sequence calculation, x * 36900, recombinant His-tagged enzyme without signal peptide, SDS-PAGE
41960
-
precusor form, encoded by the pNL2 gene, calculation from sequence of cDNA
41980
-
precusor form, encoded by the pNL3 gene, calculation from sequence of cDNA
42200
FatA open reading frames, calculated from sequence
45000
-
gel filtration
45900
x * 45900, calculated
46200
x * 46200, calculated
46500
FatB open reading frames, calculated from sequence
48080
-
sequence analysis
51000
-
isozymes AH1, AH2, TSKgel G3000SW gel filtration
53000
-
oleoyl-ACP thioesterase, gel filtration
57000
-
isozyme AH3, TSKgel G3000SW gel filtration
59000
-
isozyme AH1, gel filtration
61000
-
SDS-PAGE, recombinant protein
66000
Elaeis sp.
-
x * 66000, recombinant glutathione S-transferase fusion protein, SDS-PAGE
70000 - 80000
-
gel filtration
78000
-
gel filtration
84000
-
enzyme from leaf epidermis, gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 40000, Western blot analysis
monomer
-
1 * 42500-44000, SDS-PAGE
additional information
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
the 40 kDa protein is cleaved to a 34 kDa protein within 3 h. This degradation does not change activity, it is unknown whether this degradation is of physiological significance
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
activity relatively stable at 35°C
50
-
20 min stable
70
-
15 min, enzyme form PO-FAT is heat-stable, after 45 min the enzyme retains 30% of the original activity
80
-
15 min, 30% remaining activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol, 25%, is required for stability during purification for the enzyme form PO-FAT
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme form PO-FAT, ammonium sulfate pellet, stable
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ion exchange chromatography (DEAE), [acyl-carrier protein]-affinity chromatography
-
enzyme form PO-FAT, 499fold
-
from leaf epidermis
-
immobilized metal ion affinity chromatography (Ni2+); immobilized metal ion affinity chromatography (Ni2+)
isozyme AH1
-
native enzyme to homogeneity from developing seeds by hydroxyapatite, ion exchange, and [acyl carrier protein] affinity chromatographies, and preparative native PAGE
-
partial purification
-
partial purification of the isozymes and the recombinant chimeric mutants
-
recombinant His-tagged enzyme from Escherichia coli by metal affinity chromatography
-
to homogeneity in a single step by gel filtration; to homogeneity in a single step by gel filtration
two thioesterase activities: medium-chain acyl-ACP thioesterase and oleoyl-ACP thioesterase
Uc FatB1 and mutants
-
using affinity chromatography
-
using metal affinity chromatography
-
var. Fuerte
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a His-tagged version expressed in Escherichia coli XL-1 blue; a His-tagged version expressed in Escherichia coli XL-1 blue
coding region (including the chloroplast targeting peptide) of FATB1 cDNA amplified, then ligated into the 2S::GUS plasmid vector, using XbaI/SacI to place the gusA gene behind the seed-specific promoter. The 2S::JcFATB1 construct transferred into Agrobacterium tumefaciens GV3101, and Arabidopsis plants for overexpression
-
DNA and amino acid sequence determination and analysis, construction of a cDNA library from kernel DNA
DNA sequence determination and analysis
expressed in Escherichia coli
expressed in Escherichia coli K27fadD88
-
expressed in Escherichia coli MG1655
-
expressed in Nicotiana tabacum
-
expressed in Phaeodactylum tricornutum
expressed in Tobacco, Arabidopsis thaliana and Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli. The ectopically expressed MlFatB gene causes alteration in the fatty acid profile of Escherichia coli cells
expression of FatB as soluble enzyme in diverse Escherichia coli strains and in vitro transcription and translation lead to 2 different polypeptides by alternative initiation, a full-length 46 kDa form and a truncated 35 kDa form
expression of medium-chain acyl-acyl carrier protein thioesterase in Escherichia coli
-
expression of UcFatB1 and mutants in Escherichia coli
-
functional expression in Escherichia coli, diverse recombinant mutant strains
-
gene fatA1, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional expression as soluble His-tagged enzyme in Escherichia coli strain BL21 and DH5alpha, lipid analysis in recombinant Escherichia coli cells
-
overexpression in seeds of Arabidopsis thaliana under control of a seed-specific promotor via Agrobacterium tumefaciens infection resulting in accumulation of high amounts of palmitate, anti-sense expression of the cDNA in seeds under control of the S35 promotor from cauliflower mosaic virus leading to reduced enzyme activity in flowers and seeds but not in leaves, tissue-specific expression pattern
-
overexpression in transgenic wheat
-
overexpression of CcFATB1 in developing seeds of Arabidopsis partially redirects fatty acid synthesis toward medium-chain FA (12:0, 14:0, and 16:0). Overexpression of CcFATB1 cDNA complemented the low-palmitate (16:0) but not the low-stearate (18:0) phenotype in leaves and seeds of an Arabidopsis fatb-2 mutant; overexpression of CcFATB2 in developing seeds of Arabidopsis complements the low-palmitate (16:0) and the low-stearate (18:0) phenotype in leaves and seeds of an Arabidopsis fatb-2 mutant
overexpression of wild-type isozymes and chimeric mutants in Escherichia coli Bl21(DE3), the chimeric mutants are constructed by combination of the N-terminus of FatA with the C-terminus of FatB resulting in FatAB, or vice versa resulting in FatBA
-
PCR fragments cloned into the pMBL-T vector, subcloned into the BamHI-HindIII or SacI-KpnI sites of the pQE-80L vector. Resulting construct pQERcFatA overexpressed in Escherichia coli XL1-Blue; PCR fragments cloned into the pMBL-T vector, subcloned into the BamHI-HindIII or SacI-KpnI sites of the pQE-80L vector. Resulting construct pQERcFatB overexpressed in Escherichia coli XL1-Blue
recombinantly expressed in Escherichia coli
single gene, partial DNA sequence determination and DNA sequence analysis, expression in Escherichia coli BL21 (DE3) as glutathione S-transferase fusion protein
Elaeis sp.
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
highest expression in the developing seeds 75 days after flowering
-
highly expressed in developing seed endosperm; highly expressed in developing seed endosperm and leaf
-
is most strongly expressed in seeds, in which its expression peaks in late developmental stages
-
transcript accumulation profile is temporally regulated during embryo development. Displays maximum level of transcription in the period of maximum oil accumulation; transcript accumulation profile is temporally regulated during embryo development. Displays maximum level of transcription in the period of maximum oil accumulation
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K216A
-
site-directed mutagenesis, the mutant shows latered substrate specificity compared to the wild-type enzyme in recombinant Escherichia coli cells, lipid composition, overview
K216E
-
site-directed mutagenesis, the mutant shows latered substrate specificity compared to the wild-type enzyme in recombinant Escherichia coli cells, lipid composition, overview
L118W
-
mutant displays three orders of magnitude lower catalytic activity compared to wild-type. Km value similar to wild-type
M206W
-
mutant displays lower catalytic activity compared to wild-type. Km value similar to wild-type, only for substrate 18:1-ACP Km value highly increased compared to wild-type
Q215W
-
mutant displays equivalent or improved activities towards all substrates with marked 2 and 2.6fold increased activities for palmitoleoyl-ACP and palmitoyl-ACP, respectively, compared to wild-type. Expression of mutant in Nicotiana benthamiana leads to a higher average values of acyl-CoA. Expressed in Arabidopsis mutant displays displays a 40% decrease in oil content relative to wild-type. Mutant produces an increase in the content of saturated fatty acids, palmitic and stearic acids, with a concomitant decrease in oleic acid derivatives
R143A/K144A
-
site-directed mutagenesis, the mutant shows latered substrate specificity compared to the wild-type enzyme in recombinant Escherichia coli cells, lipid composition, overview
R143E/K144E
-
site-directed mutagenesis, the mutant shows latered substrate specificity compared to the wild-type enzyme in recombinant Escherichia coli cells, lipid composition, overview
R212A/R213A
-
site-directed mutagenesis, the mutant shows latered substrate specificity compared to the wild-type enzyme in recombinant Escherichia coli cells, lipid composition, overview
R212E/R213E
-
site-directed mutagenesis, the mutant shows latered substrate specificity compared to the wild-type enzyme in recombinant Escherichia coli cells, lipid composition, overview
T182W
-
mutant displays lower catalytic activity compared to wild-type. Km value similar to wild-type. Leaf triacylglycerols are increased 2 to 4fold when expressed in Nicotiana benthamiana compared to expression of mutant T182W and wild-type, respectively
K216A
-
site-directed mutagenesis, the mutant shows latered substrate specificity compared to the wild-type enzyme in recombinant Escherichia coli cells, lipid composition, overview
-
R143A/K144A
-
site-directed mutagenesis, the mutant shows latered substrate specificity compared to the wild-type enzyme in recombinant Escherichia coli cells, lipid composition, overview
-
R143E/K144E
-
site-directed mutagenesis, the mutant shows latered substrate specificity compared to the wild-type enzyme in recombinant Escherichia coli cells, lipid composition, overview
-
R212A/R213A
-
site-directed mutagenesis, the mutant shows latered substrate specificity compared to the wild-type enzyme in recombinant Escherichia coli cells, lipid composition, overview
-
R212E/R213E
-
site-directed mutagenesis, the mutant shows latered substrate specificity compared to the wild-type enzyme in recombinant Escherichia coli cells, lipid composition, overview
-
C320A
-
no activity
C320S
-
slightly reduced activity
H140A
-
reduced activity
H140R
-
reduced activity
H285A
-
no activity
H285R
-
reduced activity
H345A
-
reduced activity
H345R
-
reduced activity
additional information
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
the new MbFatB gene isolated from Madhuca butyracea can be used in future for transgenic development of oil-seed Brassica, a widely cultivated crop that expresses predominantly oleoyl-ACP thioesterase (FatA) in its seed tissue and has high amount of unwanted erucic acid in edible oil in order to alter the fatty acid profile in a desirable way
industry
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Show AA Sequence (406 entries)
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